Choi, Y., Kim, E., Suh, Y. (2010). Minocycline blocks c-terminal fragments of amyloid precursor protein-induced neurotoxicity by inhibition of cytochrome c release and caspase-12 activation. Iranian Journal of Pharmaceutical Research, Volume 3(Supplement 1), 82-82.
Y Choi; EM Kim; YH Suh. "Minocycline blocks c-terminal fragments of amyloid precursor protein-induced neurotoxicity by inhibition of cytochrome c release and caspase-12 activation". Iranian Journal of Pharmaceutical Research, Volume 3, Supplement 1, 2010, 82-82.
Choi, Y., Kim, E., Suh, Y. (2010). 'Minocycline blocks c-terminal fragments of amyloid precursor protein-induced neurotoxicity by inhibition of cytochrome c release and caspase-12 activation', Iranian Journal of Pharmaceutical Research, Volume 3(Supplement 1), pp. 82-82.
Choi, Y., Kim, E., Suh, Y. Minocycline blocks c-terminal fragments of amyloid precursor protein-induced neurotoxicity by inhibition of cytochrome c release and caspase-12 activation. Iranian Journal of Pharmaceutical Research, 2010; Volume 3(Supplement 1): 82-82.
Minocycline blocks c-terminal fragments of amyloid precursor protein-induced neurotoxicity by inhibition of cytochrome c release and caspase-12 activation
Minocycline is a second-generation tetracycline that effectively crosses the blood-brain barrier. It has remarkable neuroprotective qualities in models of cerebral ischaemia, traumatic brain injury, Huntington’s and Parkinson’s diseases. However, there is no evidence about neuroprotective effects of minocycline on AD. Alzheimer’s disease (AD) is a neurodegenerative disorder characterized neuropathologically by the presence of neuritic plaques containing amyloid fibrils and neurofibrillary tangles whose main component is paired helical filament composed of hyperphosphorylated tau. There are numerous lines of evidence that some of the neurotoxicity associated with AD is due to proteolytic fragments of the amyloid precursor protein (APP). In this study, it was found out that minocycline reduces neurotoxicity induced by various C-terminal fragments of APP through inhibition of cytochrome c release and caspase-12 activation.
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